Tight ligand binding affinities determined from thermodynamic linkage to temperature by titration calorimetry.

摘要: A general isothermal titration calorimetry method is described that can be used to determine equilibrium binding constants for high-affinity interactions of ligands with biological macromolecules. The exploits the thermodynamic linkage between ligand constant and temperature. By measuring enthalpy change an interaction as a function temperature directly, in affinity calculated integrated form van't Hoff equation applicable When dependence combined absolute determined independently at convenient (where most accurately or easily measured), over entire range determined.